Humoral immunity is mediated by serum antibodies which are proteins secreted by the B cell compartment of the immune response. Antibodies are a heterogeneous mixture of serum globulins, all of which share the ability to bind individually to specific antigens. All serum globulins with antibody activity are referred to as immunoglobulins.
All immunoglobulin molecules have common structural features which enable to do two things: 1) recognize and bind specifically to a unique structural entity on an antigen, and 2) perform a common biologic function after combining with the antigen. Basically, each immunoglobulin molecule consists of two identical light chains and two identical heavy chains linked by disulfide bridges.
A continuing need in the field of immunology and infectious disease, concerns the availability of highly specific and highly effective antibodies.
What is needed are effective methods and compositions for generation of highly specific and highly effective antibodies. Preferably such antibodies would recognize specific epitopes on various antigens such as amyloid protein, prion protein or P170 glycoprotein.